Abstract
Activin signals through a heteromeric complex of receptor serine kinases by inducing type II receptor-mediated phosphorylation, and consequent activation, of the type I receptor. Type I receptor phosphorylation occurs at a glycine- and serine-rich site in the juxtamembrane domain; phosphorylation at that site correlates with signaling. Investigation of type I activin receptor mutants impaired for GS domain phosphorylation revealed that, in the presence of elevated amounts of type II activin receptor, GS domain phosphorylation is not required for signaling. The type I receptor showed activin-dependent phosphorylation of several tryptic phosphopeptides, suggesting that phosphorylation of receptor I at sites both within and outside the GS domain is required for full signaling.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Activin Receptors
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Activin Receptors, Type I
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Activins
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Animals
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Cell Line
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Chromatography, Thin Layer
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Electrophoresis, Polyacrylamide Gel
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Genes, Reporter / genetics
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Inhibins / metabolism*
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Luciferases / analysis
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Luciferases / genetics
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Luciferases / metabolism
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Lung / metabolism
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Mink
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Mutation / genetics
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Phosphoamino Acids / analysis
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Phosphopeptides / analysis
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Phosphorylation
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Precipitin Tests
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Receptors, Growth Factor / chemistry
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Receptors, Growth Factor / genetics
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Receptors, Growth Factor / metabolism*
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Signal Transduction / genetics
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Signal Transduction / physiology
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Transfection / genetics
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beta-Galactosidase / analysis
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beta-Galactosidase / genetics
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beta-Galactosidase / metabolism
Substances
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Phosphoamino Acids
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Phosphopeptides
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Receptors, Growth Factor
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Activins
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Inhibins
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Luciferases
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Activin Receptors
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Activin Receptors, Type I
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beta-Galactosidase